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Conserved domains on  [gi|488141433|ref|WP_002212641|]
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ProQ/FINO family protein [Neisseria meningitidis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ProQ super family cl34553
sRNA-binding protein ProQ [Signal transduction mechanisms];
39-107 5.66e-17

sRNA-binding protein ProQ [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG3109:

Pssm-ID: 442343 [Multi-domain]  Cd Length: 153  Bit Score: 71.93  E-value: 5.66e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488141433  39 KRFKPLALGIDQDLIAALPQ--YDSALIARVLANHCRRPRYLKALARGGKRFDLNNRFKGEVTPEEQAIAQ 107
Cdd:COG3109   31 EEPKPLKIGIFQDLAARLPDdeLSKTQLRRALRRYTRSWRYLKAVKEGAQRVDLDGNPAGEVTEEHAEHAR 101
 
Name Accession Description Interval E-value
ProQ COG3109
sRNA-binding protein ProQ [Signal transduction mechanisms];
39-107 5.66e-17

sRNA-binding protein ProQ [Signal transduction mechanisms];


Pssm-ID: 442343 [Multi-domain]  Cd Length: 153  Bit Score: 71.93  E-value: 5.66e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488141433  39 KRFKPLALGIDQDLIAALPQ--YDSALIARVLANHCRRPRYLKALARGGKRFDLNNRFKGEVTPEEQAIAQ 107
Cdd:COG3109   31 EEPKPLKIGIFQDLAARLPDdeLSKTQLRRALRRYTRSWRYLKAVKEGAQRVDLDGNPAGEVTEEHAEHAR 101
ProQ smart00945
ProQ/FINO family; This family includes ProQ, which is required for full activation of the ...
 36-107 3.70e-12

ProQ/FINO family; This family includes ProQ, which is required for full activation of the osmoprotectant transporter, ProQ, in Escherichia coli.


Pssm-ID: 198013 [Multi-domain]  Cd Length: 113  Bit Score: 58.52  E-value: 3.70e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488141433    36 DVFKRFKPLALGIDQDLIAALPQ---YDSALIARVLANHCRRPRYLKALARGGKRFDLNNRFKGEVTPEEQAIAQ 107
Cdd:smart00945  21 GANGAPKPLKIGIFQDLLARLEEdekVSKTALREALRTYTRSWRYLKAVKAGAVRVDLQGNPAEEVTEEHAAHAL 95
ProQ pfam04352
ProQ/FINO family; This family includes ProQ, which is required for full activation of the ...
 40-107 5.19e-11

ProQ/FINO family; This family includes ProQ, which is required for full activation of the osmoprotectant transporter, ProP, in Escherichia coli. This family includes several bacterial fertility inhibition (FINO) proteins. The conjugative transfer of F-like plasmids is repressed by FinO, an RNA binding protein. FinO interacts with the F-plasmid encoded traJ mRNA and its antisense RNA, FinP, stabilising FinP against endonucleolytic degradation and facilitating sense-antisense RNA recognition. ProQ operates as an RNA-chaperone, binding RNA and bringing about both RNA strand-exchange and RNA duplexing. This suggests that in fact it does not regulate ProP transcription but rather regulates ProP translation through activity as an RNA-binding protein.


Pssm-ID: 461270  Cd Length: 106  Bit Score: 55.31  E-value: 5.19e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141433   40 RFKPLALGIDQDLI--AALPQYDSALIARVLANHCRRPRYLKALARGGKRFDLNNRFKGEVTPEEQAIAQ 107
Cdd:pfam04352  21 EKLPLKIGIFQDLLelADDLGLSKTQLRQALRTYTRSWRYLAAMKEGAARVDLDGNPAGEVTAEHAEHAR 90
FinO_conjug_rep cd00236
FinO bacterial conjugation repressor domain; the basic protein FinO is part of the the two ...
 41-106 3.33e-03

FinO bacterial conjugation repressor domain; the basic protein FinO is part of the the two component FinOP system which is responsible for repressing bacterial conjugation; the FinOP system represses the transfer (tra) operon of the F-plasmid which encodes the proteins responsible for conjugative transfer of this plasmid from host to recipient Escherichia coli cells; antisense RNA, FinP is thought to interact with traJ mRNA to occlude its ribosome binding site, blocking traJ translation and thereby inhibiting transcription of the tra operon; FinO protects FinP against degradation by binding to FinP and sterically blocking the cellular endonuclease RNase E; FinO also also binds to the complementary stem-loop structures in traJ mRNA and promotes duplex formation between FinP and traJ RNA in vitro; this domain contains two independent RNA binding regions


Pssm-ID: 238145  Cd Length: 146  Bit Score: 35.64  E-value: 3.33e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488141433  41 FKPLALGIDQDLIAALPQYDSALIA-----RVLANHCRRPRYLKALARGGKRFDLNNRFKGEVTPEEQAIA 106
Cdd:cd00236   56 PRLLKCGIKDGILQDVAQHPNIPLTheelrCAVKAITRRESYLQAMVAGAPRYDLEGYVAGHISQEAEVYA 126
 
Name Accession Description Interval E-value
ProQ COG3109
sRNA-binding protein ProQ [Signal transduction mechanisms];
39-107 5.66e-17

sRNA-binding protein ProQ [Signal transduction mechanisms];


Pssm-ID: 442343 [Multi-domain]  Cd Length: 153  Bit Score: 71.93  E-value: 5.66e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488141433  39 KRFKPLALGIDQDLIAALPQ--YDSALIARVLANHCRRPRYLKALARGGKRFDLNNRFKGEVTPEEQAIAQ 107
Cdd:COG3109   31 EEPKPLKIGIFQDLAARLPDdeLSKTQLRRALRRYTRSWRYLKAVKEGAQRVDLDGNPAGEVTEEHAEHAR 101
ProQ smart00945
ProQ/FINO family; This family includes ProQ, which is required for full activation of the ...
 36-107 3.70e-12

ProQ/FINO family; This family includes ProQ, which is required for full activation of the osmoprotectant transporter, ProQ, in Escherichia coli.


Pssm-ID: 198013 [Multi-domain]  Cd Length: 113  Bit Score: 58.52  E-value: 3.70e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488141433    36 DVFKRFKPLALGIDQDLIAALPQ---YDSALIARVLANHCRRPRYLKALARGGKRFDLNNRFKGEVTPEEQAIAQ 107
Cdd:smart00945  21 GANGAPKPLKIGIFQDLLARLEEdekVSKTALREALRTYTRSWRYLKAVKAGAVRVDLQGNPAEEVTEEHAAHAL 95
ProQ pfam04352
ProQ/FINO family; This family includes ProQ, which is required for full activation of the ...
 40-107 5.19e-11

ProQ/FINO family; This family includes ProQ, which is required for full activation of the osmoprotectant transporter, ProP, in Escherichia coli. This family includes several bacterial fertility inhibition (FINO) proteins. The conjugative transfer of F-like plasmids is repressed by FinO, an RNA binding protein. FinO interacts with the F-plasmid encoded traJ mRNA and its antisense RNA, FinP, stabilising FinP against endonucleolytic degradation and facilitating sense-antisense RNA recognition. ProQ operates as an RNA-chaperone, binding RNA and bringing about both RNA strand-exchange and RNA duplexing. This suggests that in fact it does not regulate ProP transcription but rather regulates ProP translation through activity as an RNA-binding protein.


Pssm-ID: 461270  Cd Length: 106  Bit Score: 55.31  E-value: 5.19e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141433   40 RFKPLALGIDQDLI--AALPQYDSALIARVLANHCRRPRYLKALARGGKRFDLNNRFKGEVTPEEQAIAQ 107
Cdd:pfam04352  21 EKLPLKIGIFQDLLelADDLGLSKTQLRQALRTYTRSWRYLAAMKEGAARVDLDGNPAGEVTAEHAEHAR 90
FinO_conjug_rep cd00236
FinO bacterial conjugation repressor domain; the basic protein FinO is part of the the two ...
 41-106 3.33e-03

FinO bacterial conjugation repressor domain; the basic protein FinO is part of the the two component FinOP system which is responsible for repressing bacterial conjugation; the FinOP system represses the transfer (tra) operon of the F-plasmid which encodes the proteins responsible for conjugative transfer of this plasmid from host to recipient Escherichia coli cells; antisense RNA, FinP is thought to interact with traJ mRNA to occlude its ribosome binding site, blocking traJ translation and thereby inhibiting transcription of the tra operon; FinO protects FinP against degradation by binding to FinP and sterically blocking the cellular endonuclease RNase E; FinO also also binds to the complementary stem-loop structures in traJ mRNA and promotes duplex formation between FinP and traJ RNA in vitro; this domain contains two independent RNA binding regions


Pssm-ID: 238145  Cd Length: 146  Bit Score: 35.64  E-value: 3.33e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488141433  41 FKPLALGIDQDLIAALPQYDSALIA-----RVLANHCRRPRYLKALARGGKRFDLNNRFKGEVTPEEQAIA 106
Cdd:cd00236   56 PRLLKCGIKDGILQDVAQHPNIPLTheelrCAVKAITRRESYLQAMVAGAPRYDLEGYVAGHISQEAEVYA 126
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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